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Database: UniProt
Entry: I1MKE0_SOYBN
LinkDB: I1MKE0_SOYBN
Original site: I1MKE0_SOYBN 
ID   I1MKE0_SOYBN            Unreviewed;       577 AA.
AC   I1MKE0;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 2.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=L-gulonolactone oxidase {ECO:0000256|ARBA:ARBA00013121};
DE            EC=1.1.3.8 {ECO:0000256|ARBA:ARBA00013121};
GN   Name=100789425 {ECO:0000313|EnsemblPlants:KRH06389};
GN   ORFNames=GLYMA_16G020000 {ECO:0000313|EMBL:KRH06389.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH06389.1};
RN   [1] {ECO:0000313|EMBL:KRH06389.1, ECO:0000313|EnsemblPlants:KRH06389}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH06389};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH06389.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRH06389}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH06389};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH06389.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH06389.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-gulono-1,4-lactone + O2 = H(+) + H2O2 + L-ascorbate;
CC         Xref=Rhea:RHEA:32363, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:17587, ChEBI:CHEBI:38290; EC=1.1.3.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00001630};
CC   -!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005147}.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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DR   EMBL; CM000849; KRH06389.1; -; Genomic_DNA.
DR   RefSeq; XP_003548404.1; XM_003548356.3.
DR   AlphaFoldDB; I1MKE0; -.
DR   SMR; I1MKE0; -.
DR   STRING; 3847.I1MKE0; -.
DR   PaxDb; 3847-GLYMA16G02270-1; -.
DR   EnsemblPlants; KRH06389; KRH06389; GLYMA_16G020000.
DR   GeneID; 100789425; -.
DR   Gramene; KRH06389; KRH06389; GLYMA_16G020000.
DR   KEGG; gmx:100789425; -.
DR   eggNOG; KOG4730; Eukaryota.
DR   HOGENOM; CLU_019762_2_0_1; -.
DR   InParanoid; I1MKE0; -.
DR   OMA; PEDHIKC; -.
DR   OrthoDB; 885025at2759; -.
DR   UniPathway; UPA00132; -.
DR   Proteomes; UP000008827; Chromosome 16.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0050105; F:L-gulonolactone oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR007173; ALO_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR010030; GULO_Plant.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   NCBIfam; TIGR01677; pln_FAD_oxido; 1.
DR   PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR   PANTHER; PTHR13878:SF175; L-GULONOLACTONE OXIDASE; 1.
DR   Pfam; PF04030; ALO; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..577
FT                   /note="L-gulonolactone oxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014578896"
FT   DOMAIN          50..230
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   577 AA;  63620 MW;  07EF311298DBD4B2 CRC64;
     MSNIAFRSTI VFLLFSAVLS TPPEDPIKCA TSENTTCTIT NSYGAFPDRS ICKAAQVLYP
     TTEQELVSVV ASATRNKTKM KVATRFSHSI PKLVCPEGEN GLLISTKYLN KILKVDVETR
     TMTVESGVTL QQLINEAAKV GLALPYAPYW WGLTIGGLMG TGAHGSTLRG KGSAVHDYVV
     ELRIVRPAGP EDGYAMVENL NEQHEDLNAA KVSLGVLGVI SQITLKLEPL FKRSITYVAK
     DDSDLGGQVV AFGDAHEFAD ITWYPSQHKA IYRVDDRVPI NTSGNGLYDF IPFRPTPSLA
     SVFIRTTEEI QESTNDANGK CIVASTASNT LITAAYGLTN NGIIFAGYPI IGFQNRLQSS
     GSCLDSLQDA LITTCAWDPR MKGLFFHQTT FSIRLSFVKS FIEDVQKLVE LEPKGLCVLG
     LYNGMLMRYV TASSAYLGHQ ENALDIDITY YRSKDPMTPR LYEDILEEVE QLGIFKYGGL
     PHWGKNRNLA FEGAIKKYKS AEYFLKVKEK YDLDGLFSST WTDQVLGLKD GVTILKDGCA
     LEGLCICLQD SHCNPSKGYY CRPGKVYKEA RVCTNLK
//
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